Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/75177
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans |
Author: | Bell, S. Dale, A. Rees, N. Wong, L. |
Citation: | Applied Microbiology and Biotechnology, 2010; 86(1):163-175 |
Publisher: | Springer-Verlag |
Issue Date: | 2010 |
ISSN: | 0175-7598 1432-0614 |
Statement of Responsibility: | Stephen G. Bell, Alison Dale, Nicholas H. Rees, Luet-Lok Wong |
Abstract: | Cytochrome P450 (CYP) enzymes of the CYP101 and CYP111 families from Novosphingobium aromaticivorans are heme monooxygenases that catalyze the hydroxylation of a range of terpenoid compounds. CYP101D1 and CYP101D2 oxidized camphor to 5-exo-hydroxycamphor. CYP101B1 and CYP101C1 oxidized beta-ionone to predominantly 3-R-hydroxy-beta-ionone and 4-hydroxy-beta-ionone, respectively. CYP111A2 oxidized linalool to 8-hydroxylinalool. Physiologically, these CYP enzymes could receive electrons from Arx, a [2Fe-2S] ferredoxin equivalent to putidaredoxin from the CYP101A1 system from Pseudomonas putida. A putative ferredoxin reductase (ArR) in the N. aromaticivorans genome, with high amino acid sequence homology to putidaredoxin reductase, has been over-produced in Escherichia coli and found to support substrate oxidation by these CYP enzymes via Arx with both high activity and coupling of product formation to NADH consumption. The ArR/Arx electron-transport chain has been co-expressed with the CYP enzymes in an E. coli host to provide in vivo whole-cell substrate oxidation systems that could produce up to 6.0 g L(-1) of 5-exo-hydroxycamphor at rates of up to 64 microM (gram of cell dry weight)(-1) min(-1). These efficient biocatalytic systems have potential uses in preparative scale whole-cell biotransformations. |
Keywords: | Cytochrome P450 Novosphingobium aromaticivorans Electron transfer Ferredoxin reductase Whole-cell biotransformations |
Rights: | © Springer-Verlag 2009 |
DOI: | 10.1007/s00253-009-2234-y |
Published version: | http://dx.doi.org/10.1007/s00253-009-2234-y |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.